Factors influencing the binding of calpain I to human erythrocyte inside-out vesicles.
The mechanism for binding of human erythrocyte calpain I to human erythrocyte inside-out vesicles was studied by immunoelectrophoretic blot analysis. Binding of calpain I to inside-out vesicles was observed both in the absence and presence of Ca2+. Moreover, in the absence of Ca2+, acidic proteins like casein, ovalbumin and calpastatin suppressed while basic proteins like arginase and lysozyme did not affect the binding of calpain I to inside-out vesicles. Here, we propose a model for the binding of calpain to the membrane.
Lee
W J
WJ
Department of Clinical Science, Kyoto University, Japan.
Adachi
Y
Y
Maki
M
M
Hatanaka
M
M
Murachi
T
T
D001119:Arginase / Q000494:pharmacology; D002118:Calcium / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000494:pharmacology; D002154:Calpain / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002364:Caseins / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D007122:Immunoelectrophoresis; D007136:Immunoglobulins / Q000494:pharmacology; D007976:Leupeptins / Q000494:pharmacology; D008954:Models, Biological; D009113:Muramidase / Q000494:pharmacology; D010047:Ovalbumin / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology
D002135:Calcium-Binding Proteins; D002364:Caseins; D007136:Immunoglobulins; D007976:Leupeptins; D011480:Protease Inhibitors; C033668:calpastatin; D010047:Ovalbumin; D009113:Muramidase; D002154:Calpain; D001119:Arginase; C032854:leupeptin; D002118:Calcium